Structure of the substrate-engaged SecA-SecY protein translocation machine

Chengying Ma, Xiaofei Wu, Dongjie Sun, Eunyong Park, Marco A. Catipovic, Tom A. Rapoport (), Ning Gao () and Long Li ()
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Chengying Ma: Peking University
Xiaofei Wu: Peking University
Dongjie Sun: Peking University
Eunyong Park: University of California-Berkeley
Marco A. Catipovic: Howard Hughes Medical Institute and Harvard Medical School
Tom A. Rapoport: Howard Hughes Medical Institute and Harvard Medical School
Ning Gao: Peking University
Long Li: Peking University

Nature Communications, 2019, vol. 10, issue 1, 1-9

Abstract: Abstract The Sec61/SecY channel allows the translocation of many proteins across the eukaryotic endoplasmic reticulum membrane or the prokaryotic plasma membrane. In bacteria, most secretory proteins are transported post-translationally through the SecY channel by the SecA ATPase. How a polypeptide is moved through the SecA-SecY complex is poorly understood, as structural information is lacking. Here, we report an electron cryo-microscopy (cryo-EM) structure of a translocating SecA-SecY complex in a lipid environment. The translocating polypeptide chain can be traced through both SecA and SecY. In the captured transition state of ATP hydrolysis, SecA’s two-helix finger is close to the polypeptide, while SecA’s clamp interacts with the polypeptide in a sequence-independent manner by inducing a short β-strand. Taking into account previous biochemical and biophysical data, our structure is consistent with a model in which the two-helix finger and clamp cooperate during the ATPase cycle to move a polypeptide through the channel.

Date: 2019
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DOI: 10.1038/s41467-019-10918-2

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